HEADER ISOMERASE 29-NOV-09 3KVC
TITLE CRYSTAL STRUCTURE OF BOVINE RPE65 AT 1.9 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOID ISOMEROHYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALL-TRANS-RETINYL-PALMITATE HYDROLASE, RETINOL ISOMERASE,
COMPND 5 RETINAL PIGMENT EPITHELIUM-SPECIFIC 65 KDA PROTEIN;
COMPND 6 EC: 3.1.1.64, 5.2.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 OTHER_DETAILS: RETINAL PIGMENT EPITHELIUM MICROSOMES
KEYWDS 7-BLADED BETA-PROPELLER, MONOTOPIC MEMBRANE PROTEIN, SENSORY
KEYWDS 2 TRANSDUCTION, VISION, ISOMERASE, NON-HEME IRON PROTEIN, ACETYLATION,
KEYWDS 3 CELL MEMBRANE, CYTOPLASM, HYDROLASE, IRON, LIPOPROTEIN, MEMBRANE,
KEYWDS 4 METAL-BINDING, PALMITATE, PHOSPHOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.D.KISER,D.T.LODOWSKI,M.GOLCZAK,K.PALCZEWSKI
REVDAT 4 06-SEP-23 3KVC 1 REMARK SEQADV
REVDAT 3 01-NOV-17 3KVC 1 REMARK
REVDAT 2 12-MAY-10 3KVC 1 JRNL
REVDAT 1 02-FEB-10 3KVC 0
JRNL AUTH M.GOLCZAK,P.D.KISER,D.T.LODOWSKI,A.MAEDA,K.PALCZEWSKI
JRNL TITL IMPORTANCE OF MEMBRANE STRUCTURAL INTEGRITY FOR RPE65
JRNL TITL 2 RETINOID ISOMERIZATION ACTIVITY.
JRNL REF J.BIOL.CHEM. V. 285 9667 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20100834
JRNL DOI 10.1074/JBC.M109.063941
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 113526
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6139
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7477
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 455
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 503
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.68000
REMARK 3 B22 (A**2) : 3.68000
REMARK 3 B33 (A**2) : -7.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.020
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.019
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.749
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8293 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5568 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11295 ; 1.455 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13600 ; 0.885 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1005 ; 6.726 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 399 ;30.809 ;24.411
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1339 ;11.831 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;13.944 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1233 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9202 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1698 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5003 ; 0.943 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1990 ; 0.254 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8163 ; 1.646 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3290 ; 2.382 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3123 ; 3.767 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.665
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : H+K,-K,-L
REMARK 3 TWIN FRACTION : 0.335
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PARAMETERS FOR MASK CACLULATION
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3KVC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056493.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03324
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMETER. ADJUSTABLE
REMARK 200 FOCUSING MIRRORS IN K-B GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119836
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : 0.10400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.56500
REMARK 200 R SYM FOR SHELL (I) : 0.56500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.260
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: DIRECT REFINEMENT
REMARK 200 STARTING MODEL: PDB ENTRY 3FSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 200 AS PRECIPITANT , PH 6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.81000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.90500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.35750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 14.45250
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.26250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 PHE A 108
REMARK 465 PRO A 109
REMARK 465 ASP A 110
REMARK 465 PRO A 111
REMARK 465 CYS A 112
REMARK 465 LYS A 113
REMARK 465 ASN A 114
REMARK 465 ILE A 115
REMARK 465 PHE A 116
REMARK 465 SER A 117
REMARK 465 ARG A 118
REMARK 465 PHE A 119
REMARK 465 PHE A 120
REMARK 465 SER A 121
REMARK 465 TYR A 122
REMARK 465 PHE A 123
REMARK 465 ARG A 124
REMARK 465 GLY A 125
REMARK 465 VAL A 126
REMARK 465 LYS A 198
REMARK 465 ASN A 199
REMARK 465 PHE A 200
REMARK 465 LEU A 261
REMARK 465 PHE A 262
REMARK 465 LYS A 263
REMARK 465 PHE A 264
REMARK 465 LEU A 265
REMARK 465 SER A 266
REMARK 465 SER A 267
REMARK 465 TRP A 268
REMARK 465 SER A 269
REMARK 465 LEU A 270
REMARK 465 TRP A 271
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 PHE B 108
REMARK 465 PRO B 109
REMARK 465 ASP B 110
REMARK 465 PRO B 111
REMARK 465 CYS B 112
REMARK 465 LYS B 113
REMARK 465 ASN B 114
REMARK 465 ILE B 115
REMARK 465 PHE B 116
REMARK 465 SER B 117
REMARK 465 ARG B 118
REMARK 465 PHE B 119
REMARK 465 PHE B 120
REMARK 465 SER B 121
REMARK 465 TYR B 122
REMARK 465 PHE B 123
REMARK 465 ARG B 124
REMARK 465 GLY B 125
REMARK 465 VAL B 126
REMARK 465 LYS B 198
REMARK 465 ASN B 199
REMARK 465 PHE B 200
REMARK 465 LEU B 261
REMARK 465 PHE B 262
REMARK 465 LYS B 263
REMARK 465 PHE B 264
REMARK 465 LEU B 265
REMARK 465 SER B 266
REMARK 465 SER B 267
REMARK 465 TRP B 268
REMARK 465 SER B 269
REMARK 465 LEU B 270
REMARK 465 TRP B 271
REMARK 465 GLY B 272
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HIS A 321 O HOH A 636 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 131 93.59 -63.02
REMARK 500 THR A 147 -136.86 -113.93
REMARK 500 THR A 149 -168.41 -105.75
REMARK 500 PHE A 196 30.75 -95.80
REMARK 500 ILE A 315 -60.43 -92.10
REMARK 500 HIS A 321 -131.01 48.23
REMARK 500 GLU A 399 -3.74 81.39
REMARK 500 THR A 432 -30.15 -131.02
REMARK 500 PHE A 442 -2.01 80.15
REMARK 500 ASP A 445 10.09 -143.05
REMARK 500 PHE A 526 -64.57 -92.81
REMARK 500 ASN B 131 94.35 -68.84
REMARK 500 THR B 147 -137.27 -117.39
REMARK 500 THR B 149 -163.09 -102.86
REMARK 500 HIS B 321 -131.10 49.13
REMARK 500 GLU B 322 31.56 -91.20
REMARK 500 GLU B 399 -4.37 77.66
REMARK 500 SER B 410 117.86 -161.14
REMARK 500 PHE B 526 -64.64 -93.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 534 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 180 NE2
REMARK 620 2 HIS A 241 NE2 91.9
REMARK 620 3 HIS A 313 NE2 104.8 95.9
REMARK 620 4 HIS A 527 NE2 93.0 162.3 99.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 B 534 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 180 NE2
REMARK 620 2 HIS B 241 NE2 94.6
REMARK 620 3 HIS B 313 NE2 104.6 97.0
REMARK 620 4 HIS B 527 NE2 90.7 162.3 97.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 534
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FSN RELATED DB: PDB
DBREF 3KVC A 1 533 UNP Q28175 RPE65_BOVIN 1 533
DBREF 3KVC B 1 533 UNP Q28175 RPE65_BOVIN 1 533
SEQADV 3KVC LEU A 341 UNP Q28175 SER 341 VARIANT
SEQADV 3KVC LEU B 341 UNP Q28175 SER 341 VARIANT
SEQRES 1 A 533 MET SER SER GLN VAL GLU HIS PRO ALA GLY GLY TYR LYS
SEQRES 2 A 533 LYS LEU PHE GLU THR VAL GLU GLU LEU SER SER PRO LEU
SEQRES 3 A 533 THR ALA HIS VAL THR GLY ARG ILE PRO LEU TRP LEU THR
SEQRES 4 A 533 GLY SER LEU LEU ARG CYS GLY PRO GLY LEU PHE GLU VAL
SEQRES 5 A 533 GLY SER GLU PRO PHE TYR HIS LEU PHE ASP GLY GLN ALA
SEQRES 6 A 533 LEU LEU HIS LYS PHE ASP PHE LYS GLU GLY HIS VAL THR
SEQRES 7 A 533 TYR HIS ARG ARG PHE ILE ARG THR ASP ALA TYR VAL ARG
SEQRES 8 A 533 ALA MET THR GLU LYS ARG ILE VAL ILE THR GLU PHE GLY
SEQRES 9 A 533 THR CYS ALA PHE PRO ASP PRO CYS LYS ASN ILE PHE SER
SEQRES 10 A 533 ARG PHE PHE SER TYR PHE ARG GLY VAL GLU VAL THR ASP
SEQRES 11 A 533 ASN ALA LEU VAL ASN ILE TYR PRO VAL GLY GLU ASP TYR
SEQRES 12 A 533 TYR ALA CYS THR GLU THR ASN PHE ILE THR LYS VAL ASN
SEQRES 13 A 533 PRO GLU THR LEU GLU THR ILE LYS GLN VAL ASP LEU CYS
SEQRES 14 A 533 ASN TYR VAL SER VAL ASN GLY ALA THR ALA HIS PRO HIS
SEQRES 15 A 533 ILE GLU ASN ASP GLY THR VAL TYR ASN ILE GLY ASN CYS
SEQRES 16 A 533 PHE GLY LYS ASN PHE SER ILE ALA TYR ASN ILE VAL LYS
SEQRES 17 A 533 ILE PRO PRO LEU GLN ALA ASP LYS GLU ASP PRO ILE SER
SEQRES 18 A 533 LYS SER GLU ILE VAL VAL GLN PHE PRO CYS SER ASP ARG
SEQRES 19 A 533 PHE LYS PRO SER TYR VAL HIS SER PHE GLY LEU THR PRO
SEQRES 20 A 533 ASN TYR ILE VAL PHE VAL GLU THR PRO VAL LYS ILE ASN
SEQRES 21 A 533 LEU PHE LYS PHE LEU SER SER TRP SER LEU TRP GLY ALA
SEQRES 22 A 533 ASN TYR MET ASP CYS PHE GLU SER ASN GLU THR MET GLY
SEQRES 23 A 533 VAL TRP LEU HIS ILE ALA ASP LYS LYS ARG LYS LYS TYR
SEQRES 24 A 533 ILE ASN ASN LYS TYR ARG THR SER PRO PHE ASN LEU PHE
SEQRES 25 A 533 HIS HIS ILE ASN THR TYR GLU ASP HIS GLU PHE LEU ILE
SEQRES 26 A 533 VAL ASP LEU CYS CYS TRP LYS GLY PHE GLU PHE VAL TYR
SEQRES 27 A 533 ASN TYR LEU TYR LEU ALA ASN LEU ARG GLU ASN TRP GLU
SEQRES 28 A 533 GLU VAL LYS LYS ASN ALA ARG LYS ALA PRO GLN PRO GLU
SEQRES 29 A 533 VAL ARG ARG TYR VAL LEU PRO LEU ASN ILE ASP LYS ALA
SEQRES 30 A 533 ASP THR GLY LYS ASN LEU VAL THR LEU PRO ASN THR THR
SEQRES 31 A 533 ALA THR ALA ILE LEU CYS SER ASP GLU THR ILE TRP LEU
SEQRES 32 A 533 GLU PRO GLU VAL LEU PHE SER GLY PRO ARG GLN ALA PHE
SEQRES 33 A 533 GLU PHE PRO GLN ILE ASN TYR GLN LYS TYR GLY GLY LYS
SEQRES 34 A 533 PRO TYR THR TYR ALA TYR GLY LEU GLY LEU ASN HIS PHE
SEQRES 35 A 533 VAL PRO ASP ARG LEU CYS LYS LEU ASN VAL LYS THR LYS
SEQRES 36 A 533 GLU THR TRP VAL TRP GLN GLU PRO ASP SER TYR PRO SER
SEQRES 37 A 533 GLU PRO ILE PHE VAL SER HIS PRO ASP ALA LEU GLU GLU
SEQRES 38 A 533 ASP ASP GLY VAL VAL LEU SER VAL VAL VAL SER PRO GLY
SEQRES 39 A 533 ALA GLY GLN LYS PRO ALA TYR LEU LEU ILE LEU ASN ALA
SEQRES 40 A 533 LYS ASP LEU SER GLU VAL ALA ARG ALA GLU VAL GLU ILE
SEQRES 41 A 533 ASN ILE PRO VAL THR PHE HIS GLY LEU PHE LYS LYS SER
SEQRES 1 B 533 MET SER SER GLN VAL GLU HIS PRO ALA GLY GLY TYR LYS
SEQRES 2 B 533 LYS LEU PHE GLU THR VAL GLU GLU LEU SER SER PRO LEU
SEQRES 3 B 533 THR ALA HIS VAL THR GLY ARG ILE PRO LEU TRP LEU THR
SEQRES 4 B 533 GLY SER LEU LEU ARG CYS GLY PRO GLY LEU PHE GLU VAL
SEQRES 5 B 533 GLY SER GLU PRO PHE TYR HIS LEU PHE ASP GLY GLN ALA
SEQRES 6 B 533 LEU LEU HIS LYS PHE ASP PHE LYS GLU GLY HIS VAL THR
SEQRES 7 B 533 TYR HIS ARG ARG PHE ILE ARG THR ASP ALA TYR VAL ARG
SEQRES 8 B 533 ALA MET THR GLU LYS ARG ILE VAL ILE THR GLU PHE GLY
SEQRES 9 B 533 THR CYS ALA PHE PRO ASP PRO CYS LYS ASN ILE PHE SER
SEQRES 10 B 533 ARG PHE PHE SER TYR PHE ARG GLY VAL GLU VAL THR ASP
SEQRES 11 B 533 ASN ALA LEU VAL ASN ILE TYR PRO VAL GLY GLU ASP TYR
SEQRES 12 B 533 TYR ALA CYS THR GLU THR ASN PHE ILE THR LYS VAL ASN
SEQRES 13 B 533 PRO GLU THR LEU GLU THR ILE LYS GLN VAL ASP LEU CYS
SEQRES 14 B 533 ASN TYR VAL SER VAL ASN GLY ALA THR ALA HIS PRO HIS
SEQRES 15 B 533 ILE GLU ASN ASP GLY THR VAL TYR ASN ILE GLY ASN CYS
SEQRES 16 B 533 PHE GLY LYS ASN PHE SER ILE ALA TYR ASN ILE VAL LYS
SEQRES 17 B 533 ILE PRO PRO LEU GLN ALA ASP LYS GLU ASP PRO ILE SER
SEQRES 18 B 533 LYS SER GLU ILE VAL VAL GLN PHE PRO CYS SER ASP ARG
SEQRES 19 B 533 PHE LYS PRO SER TYR VAL HIS SER PHE GLY LEU THR PRO
SEQRES 20 B 533 ASN TYR ILE VAL PHE VAL GLU THR PRO VAL LYS ILE ASN
SEQRES 21 B 533 LEU PHE LYS PHE LEU SER SER TRP SER LEU TRP GLY ALA
SEQRES 22 B 533 ASN TYR MET ASP CYS PHE GLU SER ASN GLU THR MET GLY
SEQRES 23 B 533 VAL TRP LEU HIS ILE ALA ASP LYS LYS ARG LYS LYS TYR
SEQRES 24 B 533 ILE ASN ASN LYS TYR ARG THR SER PRO PHE ASN LEU PHE
SEQRES 25 B 533 HIS HIS ILE ASN THR TYR GLU ASP HIS GLU PHE LEU ILE
SEQRES 26 B 533 VAL ASP LEU CYS CYS TRP LYS GLY PHE GLU PHE VAL TYR
SEQRES 27 B 533 ASN TYR LEU TYR LEU ALA ASN LEU ARG GLU ASN TRP GLU
SEQRES 28 B 533 GLU VAL LYS LYS ASN ALA ARG LYS ALA PRO GLN PRO GLU
SEQRES 29 B 533 VAL ARG ARG TYR VAL LEU PRO LEU ASN ILE ASP LYS ALA
SEQRES 30 B 533 ASP THR GLY LYS ASN LEU VAL THR LEU PRO ASN THR THR
SEQRES 31 B 533 ALA THR ALA ILE LEU CYS SER ASP GLU THR ILE TRP LEU
SEQRES 32 B 533 GLU PRO GLU VAL LEU PHE SER GLY PRO ARG GLN ALA PHE
SEQRES 33 B 533 GLU PHE PRO GLN ILE ASN TYR GLN LYS TYR GLY GLY LYS
SEQRES 34 B 533 PRO TYR THR TYR ALA TYR GLY LEU GLY LEU ASN HIS PHE
SEQRES 35 B 533 VAL PRO ASP ARG LEU CYS LYS LEU ASN VAL LYS THR LYS
SEQRES 36 B 533 GLU THR TRP VAL TRP GLN GLU PRO ASP SER TYR PRO SER
SEQRES 37 B 533 GLU PRO ILE PHE VAL SER HIS PRO ASP ALA LEU GLU GLU
SEQRES 38 B 533 ASP ASP GLY VAL VAL LEU SER VAL VAL VAL SER PRO GLY
SEQRES 39 B 533 ALA GLY GLN LYS PRO ALA TYR LEU LEU ILE LEU ASN ALA
SEQRES 40 B 533 LYS ASP LEU SER GLU VAL ALA ARG ALA GLU VAL GLU ILE
SEQRES 41 B 533 ASN ILE PRO VAL THR PHE HIS GLY LEU PHE LYS LYS SER
HET FE2 A 534 1
HET FE2 B 534 1
HETNAM FE2 FE (II) ION
FORMUL 3 FE2 2(FE 2+)
FORMUL 5 HOH *503(H2 O)
HELIX 1 1 GLY A 10 GLU A 17 5 8
HELIX 2 2 THR A 86 LYS A 96 1 11
HELIX 3 3 LEU A 168 VAL A 172 1 5
HELIX 4 4 ASP A 218 SER A 223 5 6
HELIX 5 5 TYR A 275 ASP A 277 5 3
HELIX 6 6 PHE A 336 LEU A 341 5 6
HELIX 7 7 TYR A 342 ARG A 347 1 6
HELIX 8 8 ASN A 349 ARG A 358 1 10
HELIX 9 9 ASP A 375 THR A 379 5 5
HELIX 10 10 ASN A 422 GLY A 427 1 6
HELIX 11 11 GLY B 10 GLU B 17 5 8
HELIX 12 12 THR B 86 LYS B 96 1 11
HELIX 13 13 CYS B 169 TYR B 171 5 3
HELIX 14 14 ASP B 218 SER B 223 5 6
HELIX 15 15 TYR B 275 ASP B 277 5 3
HELIX 16 16 PHE B 336 LEU B 341 5 6
HELIX 17 17 TYR B 342 ARG B 347 1 6
HELIX 18 18 ASN B 349 ALA B 357 1 9
HELIX 19 19 ASP B 375 THR B 379 5 5
HELIX 20 20 ASN B 422 GLY B 427 1 6
SHEET 1 A 5 LEU A 26 THR A 27 0
SHEET 2 A 5 HIS A 76 PHE A 83 -1 O TYR A 79 N LEU A 26
SHEET 3 A 5 ALA A 65 LYS A 73 -1 N LYS A 69 O HIS A 80
SHEET 4 A 5 GLY A 40 PRO A 47 -1 N GLY A 46 O LEU A 66
SHEET 5 A 5 HIS A 527 LYS A 532 -1 O LEU A 529 N LEU A 43
SHEET 1 B 5 HIS A 29 GLY A 32 0
SHEET 2 B 5 GLU A 512 VAL A 518 -1 O ARG A 515 N THR A 31
SHEET 3 B 5 ALA A 500 ASN A 506 -1 N ILE A 504 O VAL A 513
SHEET 4 B 5 GLY A 484 VAL A 491 -1 N SER A 488 O LEU A 503
SHEET 5 B 5 ILE A 471 SER A 474 -1 N ILE A 471 O LEU A 487
SHEET 1 C 2 GLU A 51 VAL A 52 0
SHEET 2 C 2 GLU A 55 PRO A 56 -1 O GLU A 55 N VAL A 52
SHEET 1 D 4 ASN A 135 VAL A 139 0
SHEET 2 D 4 ASP A 142 CYS A 146 -1 O TYR A 144 N TYR A 137
SHEET 3 D 4 PHE A 151 VAL A 155 -1 O THR A 153 N ALA A 145
SHEET 4 D 4 THR A 162 ASP A 167 -1 O VAL A 166 N ILE A 152
SHEET 1 E 4 HIS A 182 ILE A 183 0
SHEET 2 E 4 VAL A 189 CYS A 195 -1 O TYR A 190 N HIS A 182
SHEET 3 E 4 ALA A 203 ILE A 209 -1 O ILE A 209 N VAL A 189
SHEET 4 E 4 GLU A 224 PRO A 230 -1 O PHE A 229 N TYR A 204
SHEET 1 F 6 GLY A 244 LEU A 245 0
SHEET 2 F 6 TYR A 249 GLU A 254 -1 O VAL A 251 N GLY A 244
SHEET 3 F 6 VAL A 287 ASP A 293 -1 O TRP A 288 N GLU A 254
SHEET 4 F 6 LYS A 298 THR A 306 -1 O LYS A 298 N ASP A 293
SHEET 5 F 6 THR A 400 GLU A 404 1 O LEU A 403 N ARG A 305
SHEET 6 F 6 THR A 392 LEU A 395 -1 N ILE A 394 O TRP A 402
SHEET 1 G 2 VAL A 257 ILE A 259 0
SHEET 2 G 2 PHE A 279 SER A 281 -1 O GLU A 280 N LYS A 258
SHEET 1 H 4 PHE A 309 ASP A 320 0
SHEET 2 H 4 PHE A 323 LYS A 332 -1 O ASP A 327 N ILE A 315
SHEET 3 H 4 GLN A 362 PRO A 371 -1 O TYR A 368 N VAL A 326
SHEET 4 H 4 GLU A 406 PHE A 409 -1 O GLU A 406 N ARG A 367
SHEET 1 I 4 GLN A 414 GLN A 420 0
SHEET 2 I 4 TYR A 433 ASN A 440 -1 O TYR A 435 N GLN A 420
SHEET 3 I 4 VAL A 443 ASN A 451 -1 O VAL A 443 N ASN A 440
SHEET 4 I 4 THR A 457 TRP A 460 -1 O TRP A 460 N LEU A 447
SHEET 1 J 5 LEU B 26 THR B 27 0
SHEET 2 J 5 HIS B 76 PHE B 83 -1 O TYR B 79 N LEU B 26
SHEET 3 J 5 GLN B 64 LYS B 73 -1 N LYS B 69 O HIS B 80
SHEET 4 J 5 GLY B 40 LEU B 49 -1 N GLY B 40 O PHE B 72
SHEET 5 J 5 HIS B 527 LYS B 532 -1 O LEU B 529 N LEU B 43
SHEET 1 K 5 HIS B 29 GLY B 32 0
SHEET 2 K 5 GLU B 512 VAL B 518 -1 O GLU B 517 N HIS B 29
SHEET 3 K 5 ALA B 500 ASN B 506 -1 N ILE B 504 O VAL B 513
SHEET 4 K 5 GLY B 484 VAL B 491 -1 N SER B 488 O LEU B 503
SHEET 5 K 5 TYR B 466 PRO B 467 -1 N TYR B 466 O VAL B 491
SHEET 1 L 5 HIS B 29 GLY B 32 0
SHEET 2 L 5 GLU B 512 VAL B 518 -1 O GLU B 517 N HIS B 29
SHEET 3 L 5 ALA B 500 ASN B 506 -1 N ILE B 504 O VAL B 513
SHEET 4 L 5 GLY B 484 VAL B 491 -1 N SER B 488 O LEU B 503
SHEET 5 L 5 ILE B 471 SER B 474 -1 N VAL B 473 O VAL B 485
SHEET 1 M 2 GLU B 51 VAL B 52 0
SHEET 2 M 2 GLU B 55 PRO B 56 -1 O GLU B 55 N VAL B 52
SHEET 1 N 4 ASN B 135 VAL B 139 0
SHEET 2 N 4 ASP B 142 CYS B 146 -1 O CYS B 146 N ASN B 135
SHEET 3 N 4 PHE B 151 VAL B 155 -1 O THR B 153 N ALA B 145
SHEET 4 N 4 THR B 162 ASP B 167 -1 O VAL B 166 N ILE B 152
SHEET 1 O 4 HIS B 182 ILE B 183 0
SHEET 2 O 4 VAL B 189 CYS B 195 -1 O TYR B 190 N HIS B 182
SHEET 3 O 4 ALA B 203 ILE B 209 -1 O ILE B 209 N VAL B 189
SHEET 4 O 4 GLU B 224 PRO B 230 -1 O PHE B 229 N TYR B 204
SHEET 1 P 6 GLY B 244 LEU B 245 0
SHEET 2 P 6 TYR B 249 GLU B 254 -1 O VAL B 251 N GLY B 244
SHEET 3 P 6 VAL B 287 ASP B 293 -1 O TRP B 288 N GLU B 254
SHEET 4 P 6 LYS B 298 THR B 306 -1 O LYS B 298 N ASP B 293
SHEET 5 P 6 THR B 400 GLU B 404 1 O ILE B 401 N LYS B 303
SHEET 6 P 6 THR B 392 LEU B 395 -1 N ILE B 394 O TRP B 402
SHEET 1 Q 2 VAL B 257 ILE B 259 0
SHEET 2 Q 2 PHE B 279 SER B 281 -1 O GLU B 280 N LYS B 258
SHEET 1 R 4 PHE B 309 ASP B 320 0
SHEET 2 R 4 PHE B 323 LYS B 332 -1 O ASP B 327 N ILE B 315
SHEET 3 R 4 GLN B 362 PRO B 371 -1 O GLN B 362 N LYS B 332
SHEET 4 R 4 GLU B 406 PHE B 409 -1 O GLU B 406 N ARG B 367
SHEET 1 S 4 GLN B 414 GLN B 420 0
SHEET 2 S 4 TYR B 433 ASN B 440 -1 O TYR B 435 N GLN B 420
SHEET 3 S 4 VAL B 443 ASN B 451 -1 O LEU B 450 N ALA B 434
SHEET 4 S 4 THR B 457 TRP B 460 -1 O TRP B 460 N LEU B 447
LINK NE2 HIS A 180 FE FE2 A 534 1555 1555 2.11
LINK NE2 HIS A 241 FE FE2 A 534 1555 1555 2.14
LINK NE2 HIS A 313 FE FE2 A 534 1555 1555 2.10
LINK NE2 HIS A 527 FE FE2 A 534 1555 1555 2.11
LINK NE2 HIS B 180 FE FE2 B 534 1555 1555 2.14
LINK NE2 HIS B 241 FE FE2 B 534 1555 1555 2.16
LINK NE2 HIS B 313 FE FE2 B 534 1555 1555 2.14
LINK NE2 HIS B 527 FE FE2 B 534 1555 1555 2.14
SITE 1 AC1 4 HIS A 180 HIS A 241 HIS A 313 HIS A 527
SITE 1 AC2 4 HIS B 180 HIS B 241 HIS B 313 HIS B 527
CRYST1 176.356 176.356 86.715 90.00 90.00 120.00 P 65 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005670 0.003274 0.000000 0.00000
SCALE2 0.000000 0.006548 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011532 0.00000
(ATOM LINES ARE NOT SHOWN.)
END